(data stored in ACNUC7421 zone)

SWISSPROT: B8I9I0_METNO

ID   B8I9I0_METNO            Unreviewed;       732 AA.
AC   B8I9I0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE            EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN   Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN   OrderedLocusNames=Mnod_0188 {ECO:0000313|EMBL:ACL55233.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55233.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55233.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC       condensation and subsequent hydrolysis of acetyl-coenzyme A
CC       (acetyl-CoA) and glyoxylate to form malate and CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00078445}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = (S)-malate +
CC       CoA. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00378410}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00641, ECO:0000256|SAAS:SAAS00171973};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate
CC       from isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00378382}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078437}.
CC   -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572,
CC       ECO:0000256|SAAS:SAAS00559604}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
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DR   EMBL; CP001349; ACL55233.1; -; Genomic_DNA.
DR   RefSeq; WP_015926946.1; NC_011894.1.
DR   ProteinModelPortal; B8I9I0; -.
DR   STRING; 460265.Mnod_0188; -.
DR   EnsemblBacteria; ACL55233; ACL55233; Mnod_0188.
DR   KEGG; mno:Mnod_0188; -.
DR   eggNOG; ENOG4107QP3; Bacteria.
DR   eggNOG; COG2225; LUCA.
DR   HOGENOM; HOG000220740; -.
DR   KO; K01638; -.
DR   OMA; GDEMHTS; -.
DR   OrthoDB; POG091H05P0; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   HAMAP; MF_00641; Malate_synth_G; 1.
DR   InterPro; IPR011076; Malate_synth-like.
DR   InterPro; IPR001465; Malate_synthase.
DR   InterPro; IPR006253; Malate_synthG.
DR   Pfam; PF01274; Malate_synthase; 1.
DR   SUPFAM; SSF51645; SSF51645; 1.
DR   TIGRFAMs; TIGR01345; malate_syn_G; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8I9I0.
DR   SWISS-2DPAGE; B8I9I0.
KW   Acyltransferase {ECO:0000313|EMBL:ACL55233.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078450};
KW   Glyoxylate bypass {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078429};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078439};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078435};
KW   Oxidation {ECO:0000256|HAMAP-Rule:MF_00641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00455574,
KW   ECO:0000313|EMBL:ACL55233.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078455}.
FT   REGION      124    125       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   REGION      456    459       Glyoxylate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    339    339       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   ACT_SITE    629    629       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   METAL       431    431       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   METAL       459    459       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     117    117       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   BINDING     275    275       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     312    312       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     339    339       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     431    431       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     540    540       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   MOD_RES     615    615       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
SQ   SEQUENCE   732 AA;  80113 MW;  C553219D99CFDD80 CRC64;
     MDRQTVSGLK VARVLHDFVV REALPGTGVS PEVFWGGLAA ILRDLTPKNR ALLAKRDALQ
     DRIDAWHRER VGRPIDAAEY ERFLREIGYL LPDPGPVKAR TENVDDEIAT IAGPQLVVPV
     SNARYALNAA NARWGSLYDA FYGTDAISEE GGATRGPGYN RTRGARVVTR ARAFLDRTVP
     LAGGRHADVV TYAVENGGLV GNMNTGETIP LARPEAFVGY RGRASMPSAL LLRHNGLHIE
     IVLDRTHRIG RFDASGVADI LIESAISTIM DLEDSVAAVD ADDKVEVYRN WLGLMNGTLS
     ARFEKDGRVM ERRLNPDRHY TAPNGGEVTV PGRSLMLVRN VGHHMVTDAV LDAEGNEVPE
     GILDAAVTAM IAIHDLRNES GLRNSRKGSV YIVKPKMHGP EEVAFAVELF GRVEAMLGLE
     RNTLKMGIMD EERRTTVNLA ACIKAADERV VFINTGFLDR TGDEIHTAME AGPVIRKNDM
     KATPWIKGYE ENNVDVGLAC GLLGRAQIGK GMWAAPDAMA DMLMQKGAHP KAGASTAWVP
     SPTAATLHAL HYHETDVHAR QEELARRPRS ALAEILQIPL ARSNFAPDDV QQEIDNNAQS
     ILGYVVRWID QGVGCSKVPD IHDVGLMEDR ATLRISSQHI ANWLHHGVVS EEQVVETLKR
     MAKVVDRQNA GDPLYRPMAP AFDGPAFRAA CDLVFKGRVQ PNGYTEWILH ARRREAKAAG
     APTEKAREGA TA
//

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